Survivin/BIRC5 Antibody (YA665)

(Synonyms: BIRC5; API4; IAP4; Baculoviral IAP repeat-containing protein 5; Apoptosis inhibitor 4; Apoptosis inhibitor survivin)

Survivin/BIRC5 Antibody (YA665) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Survivin/BIRC5.

For research use only. We do not sell to patients.
  • Host:

    Mouse

  • Isotype:

    IgG

  • Application:

    WB, IHC-P

  • Reactivity :

    Human, Rat

  • Formulation:

    Supplied in 1*PBS (pH 7.3), 50% glycerol and 0.5% BSA. Preservative: 0.02% sodium azide.

  • Conjugation:
    Non-conjugated

Applications

Application
WB Info
WB: Western Blot
IHC-P Info
IHC-P: Immunohistochemistry-Paraffin
Dilution Ratio 1:500-1:1000 1:50-1:100

Product Details

Description

Survivin/BIRC5 Antibody (YA665) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Survivin/BIRC5.

  • Host Mouse
  • Clonality Monoclonal
  • Species Reactivity
    Human, Rat
  • Observed Molecular Weight
    Observed band size: 16 kDa Info
    Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
  • Calculated Molecular Weight Predicted band size: 16 kDa
Species Reactivity Database
Immunogen

Synthetic peptide corresponding to Survivin.The exact sequence is proprietary to MCE.

Sensitivity

Endogenous

Purification

affinity purified

Conjugation

Non-conjugated

Modification

Unmodified

Isotype

IgG

Product Properties

  • Appearance

    Solution

  • Formulation

    Supplied in 1*PBS (pH 7.3), 50% glycerol and 0.5% BSA. Preservative: 0.02% sodium azide.

  • Storage & Stability

    Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

  • Shipping

    Shipping with blue ice.

Background

  • Function

    Survivin/BIRC5 is a Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Essential for the maintenance of mitochondrial integrity and function. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform[1][2][3][4][5][6][7][8][9][10][11][12][13].

  • Subcellular Localization

    Cytoplasm; Nucleus; Chromosome; Chromosome, centromere; Cytoplasm, cytoskeleton, spindle; Chromosome, centromere, kinetochore; Midbody

  • Expression


    Tissue_specificity:It is expressed only in the fetal kidney and liver, and less frequently in the lung and brain (PubMed: 10626797) . It is highly expressed in adenocarcinomas (lung, pancreatic, colon, breast, and prostate cancers) and high-grade lymphomas (PubMed: 14741722, PubMed: 16329164) . It is also expressed in various renal cell carcinoma lines (PubMed: 10626797) . It is expressed in the cochlea, including the organ of Corti, lateral walls, marginal interdental cells, as well as Schwann cells, cochlear neurons, and spiral ganglion cells (protein level) . It is not expressed in the internal sulcus, external sulcus cells, or Reissner's membrane cells (protein level) (PubMed: 20627126, PubMed: 21364656) .

    Induction:Up-regulated by COMP

  • Isoforms & Post-Translational Modification

    O15392 has 7 isomers: O15392-1: 16389 Da (predicted); O15392-2: 18636 Da (predicted); O15392-3: 15622 Da (predicted); O15392-4: 13812 Da (predicted); O15392-5: 13467 Da (predicted); O15392-6: 8991 Da (predicted); O15392-7: 8490 Da (predicted).
    Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting. Deubiquitinated by USP35 or USP38; leading to stabilization (PubMed:34438346);In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes (PubMed:14610074). Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities (PubMed:21252625). Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity (PubMed:24866247). Phosphorylation at Ser-20 by AURKC is critical for regulation of proper chromosome alignment and segregation, and possibly cytokinesis;Acetylation at Lys-129 by CBP results in its homodimerization, while deacetylation promotes the formation of monomers which heterodimerize with XPO1/CRM1 which facilitates its nuclear export. The acetylated form represses STAT3 transactivation. The dynamic equilibrium between its acetylation and deacetylation at Lys-129 determines its interaction with XPO1/CRM1, its subsequent subcellular localization, and its ability to inhibit STAT3 transactivation

  • Subunit

    Monomer or homodimer. Exists as a homodimer in the apo state and as a monomer in the CPC-bound state. The monomer protects cells against apoptosis more efficiently than the dimer.

  • SwissProt ID

    O15392

  • Gene ID
    332 [NCBI]
  • Synonyms

    BIRC5; API4; IAP4; Baculoviral IAP repeat-containing protein 5; Apoptosis inhibitor 4; Apoptosis inhibitor survivin

  • Research Field

    Cell Biology

[1]. Habtemichael N, et al. Expression analysis suggests a potential cytoprotective role of Birc5 in the inner ear. Mol Cell Neurosci. 2010 Nov;45(3):297-305. [Content Brief]

[2]. Knauer SK, et al. An otoprotective role for the apoptosis inhibitor protein survivin. Cell Death Dis. 2010 Jul 1;1(7):e51. [Content Brief]

[3]. Liu Y, et al. The Proapoptotic F-box Protein Fbxl7 Regulates Mitochondrial Function by Mediating the Ubiquitylation and Proteasomal Degradation of Survivin. J Biol Chem. 2015 May 8;290(19):11843-52. [Content Brief]

[4]. Kamran M, et al. Aurora kinase A regulates Survivin stability through targeting FBXL7 in gastric cancer drug resistance and prognosis. Oncogenesis. 2017 Feb 20;6(2):e298. [Content Brief]

[5]. Li F, et al. Control of apoptosis and mitotic spindle checkpoint by survivin. Nature. 1998 Dec 10;396(6711):580-4. [Content Brief]

[6]. Vong QP, et al. Chromosome alignment and segregation regulated by ubiquitination of survivin. Science. 2005 Dec 2;310(5753):1499-504. [Content Brief]

[7]. Wang H, et al. Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity. J Biol Chem. 2010 Nov 12;285(46):36129-37. [Content Brief]

[8]. Yamagishi Y, et al. Two histone marks establish the inner centromere and chromosome bi-orientation. Science. 2010 Oct 8;330(6001):239-43. [Content Brief]

[9]. Xia F, et al. A survivin-ran complex regulates spindle formation in tumor cells. Mol Cell Biol. 2008 Sep;28(17):5299-311. [Content Brief]

[10]. Mahotka C, et al. Survivin-deltaEx3 and survivin-2B: two novel splice variants of the apoptosis inhibitor survivin with different antiapoptotic properties. Cancer Res. 1999 Dec 15;59(24):6097-102. [Content Brief]

[11]. Pavlyukov MS, et al. Survivin monomer plays an essential role in apoptosis regulation. J Biol Chem. 2011 Jul 1;286(26):23296-307. [Content Brief]

[12]. Marusawa H, et al. HBXIP functions as a cofactor of survivin in apoptosis suppression. EMBO J. 2003 Jun 2;22(11):2729-40. [Content Brief]

[13]. Noton EA, et al. Molecular analysis of survivin isoforms: evidence that alternatively spliced variants do not play a role in mitosis. J Biol Chem. 2006 Jan 13;281(2):1286-95. [Content Brief]

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